GUAC_BACAN
ID GUAC_BACAN Reviewed; 327 AA.
AC Q81JJ9; Q6HQ42; Q6KJI6;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000255|HAMAP-Rule:MF_01511};
GN OrderedLocusNames=BA_5705, GBAA_5705, BAS5309;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP
CC to IMP. It functions in the conversion of nucleobase, nucleoside and
CC nucleotide derivatives of G to A nucleotides, and in maintaining the
CC intracellular balance of A and G nucleotides. {ECO:0000255|HAMAP-
CC Rule:MF_01511}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01511}.
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DR EMBL; AE016879; AAP29337.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34865.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57596.1; -; Genomic_DNA.
DR RefSeq; NP_847851.1; NC_003997.3.
DR RefSeq; WP_000528705.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031546.1; NC_005945.1.
DR PDB; 1YPF; X-ray; 1.80 A; A/B=1-327.
DR PDB; 2A1Y; X-ray; 2.27 A; A=1-327.
DR PDBsum; 1YPF; -.
DR PDBsum; 2A1Y; -.
DR AlphaFoldDB; Q81JJ9; -.
DR SMR; Q81JJ9; -.
DR STRING; 260799.BAS5309; -.
DR DNASU; 1085456; -.
DR EnsemblBacteria; AAP29337; AAP29337; BA_5705.
DR EnsemblBacteria; AAT34865; AAT34865; GBAA_5705.
DR GeneID; 45025280; -.
DR KEGG; ban:BA_5705; -.
DR KEGG; bar:GBAA_5705; -.
DR KEGG; bat:BAS5309; -.
DR PATRIC; fig|198094.11.peg.5667; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_0_9; -.
DR OMA; AYKEYFG; -.
DR EvolutionaryTrace; Q81JJ9; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01511; GMP_reduct_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR InterPro; IPR005994; GuaC_type_2.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..327
FT /note="GMP reductase"
FT /id="PRO_0000093746"
FT ACT_SITE 175
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT BINDING 204..227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1YPF"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1YPF"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:1YPF"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1YPF"
SQ SEQUENCE 327 AA; 36076 MW; 8006FDFA6A5F2E78 CRC64;
MGNVFDYEDI QLIPAKCIVN SRSECDTTVT LGKHKFKLPV VPANMQTIID ERIATYLAEN
NYFYIMHRFQ PEKRISFIRD MQSRGLIASI SVGVKEDEYE FVQQLAAEHL TPEYITIDIA
HGHSNAVINM IQHIKKHLPE SFVIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK
TGFGTGGWQL AALRWCAKAA SKPIIADGGI RTNGDVAKSI RFGATMVMIG SLFAGHEESP
GETIEKDGKL YKEYFGSASE FQKGEKKNVE GKKMFVEHKG SLEDTLIEME QDLQSSISYA
GGTKLDSIRT VDYVVVKNSI FNGDKVY
